Strain conformation controls the specificity of cross-species prion transmission in the yeast model

Abstract

Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause
neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast.
Cross-species prion transmission is frequently impaired, due to sequence differences in prion-
forming proteins. Recent studies of prion species barrier on the model of closely related yeast
species show that colocalization of divergent proteins is not sufficient for the cross-species prion
transmission, and that an identity of specific amino acid sequences and a type of prion
conformational variant (strain) play a major role in the control of transmission specificity. In
contrast, chemical compounds primarily influence transmission specificity via favoring certain
strain conformations, while the species origin of the host cell has only a relatively minor input.
Strain alterations may occur during cross-species prion conversion in some combinations. The
model is discussed which suggests that different recipient proteins can

title = "Strain conformation controls the specificity of cross-species prion transmission in the yeast model",

abstract = "Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast. Cross-species prion transmission is frequently impaired, due to sequence differences in prion- forming proteins. Recent studies of prion species barrier on the model of closely related yeast species show that colocalization of divergent proteins is not sufficient for the cross-species prion transmission, and that an identity of specific amino acid sequences and a type of prion conformational variant (strain) play a major role in the control of transmission specificity. In contrast, chemical compounds primarily influence transmission specificity via favoring certain strain conformations, while the species origin of the host cell has only a relatively minor input. Strain alterations may occur during cross-species prion conversion in some combinations. The model is discussed which suggests that different recipient proteins can",

N2 - Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause
neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast.
Cross-species prion transmission is frequently impaired, due to sequence differences in prion-
forming proteins. Recent studies of prion species barrier on the model of closely related yeast
species show that colocalization of divergent proteins is not sufficient for the cross-species prion
transmission, and that an identity of specific amino acid sequences and a type of prion
conformational variant (strain) play a major role in the control of transmission specificity. In
contrast, chemical compounds primarily influence transmission specificity via favoring certain
strain conformations, while the species origin of the host cell has only a relatively minor input.
Strain alterations may occur during cross-species prion conversion in some combinations. The
model is discussed which suggests that different recipient proteins can

AB - Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause
neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast.
Cross-species prion transmission is frequently impaired, due to sequence differences in prion-
forming proteins. Recent studies of prion species barrier on the model of closely related yeast
species show that colocalization of divergent proteins is not sufficient for the cross-species prion
transmission, and that an identity of specific amino acid sequences and a type of prion
conformational variant (strain) play a major role in the control of transmission specificity. In
contrast, chemical compounds primarily influence transmission specificity via favoring certain
strain conformations, while the species origin of the host cell has only a relatively minor input.
Strain alterations may occur during cross-species prion conversion in some combinations. The
model is discussed which suggests that different recipient proteins can